The investigation of the internal dynamics of the B1 IGg-binding domain of streptoccocal protein G was successfully concluded. The temperature-dependent conformational (ring-puckering) studies of fluorinated dideoxynucleosides was completed for a large number of congeners. New, recently synthesized compounds will be analyzed. Progress in obtaining NOE distance constraints for a cyclic phosphorylated tyrosine-containing peptide, designed as an SH2 binding antagonist, has yielded the first approximation of what the conformation of this peptide is likely to be in solution. The final conformation is being refined. Other cyclic peptides containing phosphonate groups in replacement of the labile phosphate group will be investigated. The solution conformation of the recently synthesized glycopeptide Ser- Ile-Lys-Val-Ala-Val-Ser-mannose, designed to inhibit carbohydrate- mediated cell to cell adhesion, will be analyzed along with other analogues bearing different sugars (lactose, N-acetylglucosamine, etc.).